Positive Well-Being, Work-Related Rumination and Work Engagement among Chinese University Logistics Staff.

Logistics personnel in Chinese universities are facing unbalanced costs and benefit from overloaded work with minimum wages, which impede school development and their well-being. However, the logistics staff population has been neglected in past investigations pertaining to psychological health conditions. The present study aimed to examine the positive well-being, work-related rumination, and work engagement of logistics staff, their correlations, and the factors affecting well-being in 282 Chinese university logistics staff via the Smith Well-being Questionnaire, the Work-Related Rumination Questionnaire, and the Utrecht Work Engagement Scale. The results indicated low levels of well-being and high levels of work-related rumination and work engagement among Chinese university logistics staff. The presence of positive attitudes towards life and work and high levels of work engagement predicts enhanced well-being, while the presence of negative characteristics and work-related rumination predicts decreased well-being. In situations where the working hours and work duties are challenging to change, universities can regularly schedule psychological counselling sessions for logistics staff to improve their well-being.

Dual roles of the Arabidopsis PEAT complex in histone H2A deubiquitination and H4K5 acetylation.

Histone H2A monoubiquitination is associated with transcriptional repression and needs to be removed by deubiquitinases to facilitate gene transcription in eukaryotes. However, the deubiquitinase responsible for genome-wide H2A deubiquitination in plants has yet to be identified. In this study, we found that the previously identified PWWP-EPCR-ARID-TRB (PEAT) complex components interact with both the ubiquitin-specific protease UBP5 and the redundant histone acetyltransferases HAM1 and HAM2 (HAM1/2) to form a larger version of PEAT complex in Arabidopsis thaliana. UBP5 functions as an H2A deubiquitinase in a nucleosome substrate-dependent manner in vitro and mediates H2A deubiquitination at the whole-genome level in vivo. HAM1/2 are shared subunits of the PEAT complex and the conserved NuA4 histone acetyltransferase complex, and are responsible for histone H4K5 acetylation. Within the PEAT complex, the PWWP components (PWWP1, PWWP2, and PWWP3) directly interact with UBP5 and are necessary for UBP5-mediated H2A deubiquitination, while the EPCR components (EPCR1 and EPCR2) directly interact with HAM1/2 and are required for HAM1/2-mediated H4K5 acetylation. Collectively, our study not only identifies dual roles of the PEAT complex in H2A deubiquitination and H4K5 acetylation but also illustrates how these processes collaborate at the whole-genome level to regulate the transcription and development in plants.

Nucleus-Targeting Nanoplatform Based on Dendritic Peptide for Precise Photothermal Therapy.

Photothermal therapy directly acting on the nucleus is a potential anti-tumor treatment with higher killing efficiency. However, in practical applications, it is often difficult to achieve precise nuclear photothermal therapy because agents are difficult to accurately anchor to the nucleus. Therefore, it is urgent to develop a nanoheater that can accurately locate the nucleus. Here, we designed an amphiphilic arginine-rich dendritic peptide (RDP) with the sequence CRRK(RRCG(Fmoc))2, and prepared a nucleus-targeting nanoplatform RDP/I by encapsulating the photothermal agent IR780 in RDP for precise photothermal therapy of the tumor nucleus. The hydrophobic group Fmoc of the dendritic peptide provides strong hydrophobic force to firmly encapsulate IR780, which improves the solubility and stability of IR780. Moreover, the arginine-rich structure facilitates cellular uptake of RDP/I and endows it with the ability to quickly anchor to the nucleus. The nucleus-targeting nanoplatform RDP/I showed efficient nuclear enrichment ability and a significant tumor inhibition effect.

3D-Printed scaffolds based on poly(Trimethylene carbonate), poly(ε-Caprolactone), and ß-Tricalcium phosphate.

Three-dimensional (3D)-printed scaffolds of biodegradable polymers have been increasingly applied in bone repair and regeneration, which helps avoid the second surgery. PTMC/PCL/TCP composites were made using poly(trimethylene carbonate), poly(ε-caprolactone), and ß-tricalcium phosphate. PTMC/PCL/TCP scaffolds were manufactured using a biological 3D printing technique. Furthermore, the properties of PTMC/PCL/TCP scaffolds, such as biodegradation, mechanic properties, drug release, cell cytotoxicity, cell proliferation, and bone repairing capacity, were evaluated. We showed that PTMC/PCL/TCP scaffolds had low cytotoxicity and good biocompatibility, and they also enhanced the proliferation of osteoblast MC3T3-E1 and rBMSC cell lines, which demonstrated improved adhesion, penetration, and proliferation. Moreover, PTMC/PCL/TCP scaffolds can enhance bone induction and regeneration, indicating that they can be used to repair bone defects in vivo.

Dual-modal polypeptide-containing contrast agents for magnetic resonance/fluorescence imaging.

Dual-modal magnetic resonance/fluorescent imaging (MRI/FI) attracts moreandmoreattentions in diagnosis of tumors. A corresponding dual-modal imaging agent with sufficient tumor sensitivity and specificity should be matched to improve imaging quality. Tripeptide (RGD) and pentapeptide (YIGSR) were selected as the tumor-targeting groups and attached to gadolinium diethylenetriaminepentaacetic acid (Gd-DTPA) and rhodamine B (RhB), and then make two novel polypeptide-based derivatives (RGD-Gd-DTPA-RhB and YIGSR-Gd-DTPA-RhB), respectively. These derivatives were further characterized and their properties, such as cell uptake, cell cytotoxicity, MRI and FI assay, were measured. YIGSR-Gd-DTPA-RhB and RGD-Gd-DTPA-RhB had high relaxivity, good tumor-targeting property, low cell cytotoxicity and good red FI in B16F10 melanoma cells. Moreover, YIGSR-Gd-DTPA-RhB and RGD-Gd-DTPA-RhB possessed high uptake to B16F10 melanoma, and then achieve highly enhanced FI and MRI of tumors in mice for a prolonged time. Therefore, YIGSR-Gd-DTPA-RhB and RGD-Gd-DTPA-RhB can be applied as the potential agents for tumor targeted MRI/FI in vivo.

The Arabidopsis NuA4 histone acetyltransferase complex is required for chlorophyll biosynthesis and photosynthesis.

Although two Enhancer of Polycomb-like proteins, EPL1A and EPL1B (EPL1A/B), are known to be conserved and characteristic subunits of the NuA4-type histone acetyltransferase complex in Arabidopsis thaliana, the biological function of EPL1A/B and the mechanism by which EPL1A/B function in the complex remain unknown. Here, we report that EPL1A/B are required for the histone acetyltransferase activity of the NuA4 complex on the nucleosomal histone H4 in vitro and for the enrichment of histone H4K5 acetylation at thousands of protein-coding genes in vivo. Our results suggest that EPL1A/B are required for linking the NuA4 catalytic subunits HISTONE ACETYLTRANSFERASE OF THE MYST FAMILY 1（HAM1) and HAM2 with accessory subunits in the NuA4 complex. EPL1A/B function redundantly in regulating plant development especially in chlorophyll biosynthesis and de-etiolation. The EPL1A/B-dependent transcription and H4K5Ac are enriched at genes involved in chlorophyll biosynthesis and photosynthesis. We also find that EAF6, another characteristic subunit of the NuA4 complex, contributes to de-etiolation. These results suggest that the Arabidopsis NuA4 complex components function as a whole to mediate histone acetylation and transcriptional activation specifically at light-responsive genes and are critical for photomorphogenesis.

Exploring the mode of binding between butylated hydroxyanisole with bovine serum albumin: Multispectroscopic and molecular docking study.

Considering the harm of BHA on humans, thorough research of the effect of BHA on the structure of serum albumin is necessary. The binding mechanisms of BHA with bovine serum albumin (BSA) and the effects of other three food additives (butylated hydroxytoluene, benzoic acid and citric acid) on BHA-BSA system were researched by multispectroscopy and molecular docking. The fluorescence quenching experiment results showed that the fluorescence quenching mechanism of BSA by BHA was static quenching. The binding constant ((5.70 ± 0.38) × 103 M-1 at 298 K) and thermodynamic parameters (ΔH = 110.8 ± 2.91 kJ·mol-1 and ΔS = 443.3 ± 9.30 J·mol-1·K-1) indicated that BHA and BSA formed a relatively stable complex through hydrophobic interaction. Three-dimensional fluorescence spectra confirmed the conformation changes of BSA due to the binding of BHA. Site marker competitive experiments and molecular docking proved that BHA could bind BSA into site I in subdomain IIA. The results of molecular docking showed that BHA formed hydrophobic interactions with amino acid residues (Ala290, Leu237, Leu259, Ile263 and Ile289). The presence of other food additives weakened the binding of BHA to BSA.

Investigation of the binding interactions between 17α-ethinylestradiol with bovine serum albumin by multispectroscopy.

To understand the effect of 17α-ethinylestradiol (EE2) on the conformation changes of bovine serum albumin (BSA), the binding mechanisms of EE2 with BSA were investigated by fluorescence spectroscopy, time-resolved fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, UV-visible spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. The quenching constants, binding constants, the number of binding sites, thermodynamic parameters, binding distance and the secondary structure changes of BSA were determined. The results of fluorescence quenching experiment suggested that the fluorescence quenching of BSA by EE was due to the formation of complex through static quenching, which was also confirmed by time-resolved fluorescence measurements. The thermodynamic parameters indicated that the binding of EE2 to BSA was driven mainly by van der Waals forces and hydrogen bonding. The conformation alterations of BSA upon EE2 binding were studied by UV-vis spectroscopy and CD spectroscopy. The results of site marker competitive experiments and molecular docking showed that the binding sites of EE2 were mainly located within site I in the subdomain IIA of BSA.

Investigation on the interaction between triclosan and bovine serum albumin by spectroscopic methods.

Multi-spectroscopic and molecular docking methods were used to study the interaction between triclosan (TCS) and bovine serum albumin (BSA). The results indicated that the fluorescence quenching of BSA by TCS was due to the formation of TCS-BSA complex through static quenching. This result was also demonstrated by time-resolved fluorescence experiment. The binding constants and number of binding sites between TCS and BSA were 1.30 × 105 M-1 and 1.17 at 298 K, respectively. The thermodynamic parameters were studied in detail which suggested that hydrophobic forces and hydrogen bond played major roles in the TCS-BSA interaction. Moreover, the site marker competitive experiments and docking studies revealed that TCS could bind BSA into site I in subdomain IIA. All the results of UV-vis spectrophotometry, circular dichroism spectroscopy and synchronous fluorescence spectroscopy showed that interaction between TCS and BSA induced conformation changes of BSA.